OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Ubiquitinomics: History, methods, and applications in basic research and drug discovery
Martin Steger, Özge Karayel, Vadim Demichev
PROTEOMICS (2022) Vol. 22, Iss. 15-16
Open Access | Times Cited: 15

Showing 15 citing articles:

Non-lysine ubiquitylation: Doing things differently
Ian R. Kelsall
Frontiers in Molecular Biosciences (2022) Vol. 9
Open Access | Times Cited: 44

Targeted Protein Degradation: Advances, Challenges, and Prospects for Computational Methods
Barmak Mostofian, Holli‐Joi Martin, Asghar M. Razavi, et al.
Journal of Chemical Information and Modeling (2023) Vol. 63, Iss. 17, pp. 5408-5432
Open Access | Times Cited: 28

CUL4-Based Ubiquitin Ligases in Chromatin Regulation: An Evolutionary Perspective
Makiko Nakagawa, Tadashi Nakagawa
Cells (2025) Vol. 14, Iss. 2, pp. 63-63
Open Access | Times Cited: 1

Proteomic approaches advancing targeted protein degradation
Gajanan Sathe, Gopal P. Sapkota
Trends in Pharmacological Sciences (2023) Vol. 44, Iss. 11, pp. 786-801
Open Access | Times Cited: 22

Phosphodegrons in Health and Disease: From Cellular Homeostasis to Therapeutic Potential
Tadashi Nakagawa, Makiko Nakagawa
Kinases and Phosphatases (2025) Vol. 3, Iss. 1, pp. 3-3
Open Access

Does the Ubiquitination Degradation Pathway Really Reach inside of the Chloroplast? A Re-Evaluation of Mass Spectrometry-Based Assignments of Ubiquitination
Klaas J. van Wijk, Mark Leppert, Zhi Sun, et al.
Journal of Proteome Research (2023) Vol. 22, Iss. 6, pp. 2079-2091
Closed Access | Times Cited: 8

Deciphering non-canonical ubiquitin signaling: biology and methodology
Nila van Overbeek, Tim Aguirre, Gerbrand J. van der Heden van Noort, et al.
Frontiers in Molecular Biosciences (2024) Vol. 10
Open Access | Times Cited: 2

Proteome Birthdating Reveals Age-Selectivity of Protein Ubiquitination
Michael E. Meadow, Sarah Broas, Margaret Hoare, et al.
Molecular & Cellular Proteomics (2024) Vol. 23, Iss. 7, pp. 100791-100791
Open Access | Times Cited: 2

Deciphering the protein ubiquitylation system in plants
Zhihua Hua
Journal of Experimental Botany (2023) Vol. 74, Iss. 21, pp. 6487-6504
Closed Access | Times Cited: 5

Proteogenomics in Cancer: Then and Now
Xiuyun Wang, Yan‐Ming Xu, Andy T. Y. Lau
Journal of Proteome Research (2023) Vol. 22, Iss. 10, pp. 3103-3122
Closed Access | Times Cited: 5

Ubiquitylomics: An Emerging Approach for Profiling Protein Ubiquitylation in Skeletal Muscle
Samuel O. Lord, Harvey E. Johnston, Rahul S. Samant, et al.
Journal of Cachexia Sarcopenia and Muscle (2024)
Open Access | Times Cited: 1

Exploration of Diagnostic Deubiquitinating Enzymes in Endometriosis and Its Immune Infiltration
Xinyun Yang, Kai Yan, Qitao Zhan, et al.
Biochemical Genetics (2024)
Closed Access

Ubiquitin diGly peptide enrichment and LC-MS/MS analysis to characterize the ubiquitinated proteome of mammalian cells
Karuppuchamy Selvaprakash, Michael Henry, Paula Meleady
Elsevier eBooks (2024), pp. 189-197
Closed Access

Proteome birthdating reveals age-selectivity of protein ubiquitination
Michael E. Meadow, Sarah Broas, Margaret Hoare, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access

Dissecting Ubiquitylation and DNA Damage Response Pathways in the Yeast Saccharomyces cerevisiae Using a Proteome-Wide Approach
Ewa Błaszczak, Emeline Pasquier, Gaëlle Le Dez, et al.
Molecular & Cellular Proteomics (2023) Vol. 23, Iss. 1, pp. 100695-100695
Open Access

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